Structure of BCR-homology (BH) domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Mar 1997.
Explore 1PBW in 3D Show helices and sheets RCSB PDB PDBe
1PBW contains 23 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 118-121 | 4 | |
| α-helix | 130-143 | 14 | |
| α-helix | 160-164 | 5 | |
| α-helix | 174-176 | 3 | |
| β-strand | 177 | 1 | 1 |
| α-helix | 179-191 | 13 | |
| α-helix | 200-209 | 10 | |
| α-helix | 210-212 | 3 | |
| α-helix | 216-227 | 12 | |
| α-helix | 234-252 | 19 | |
| α-helix | 254-257 | 4 | |
| α-helix | 261-273 | 13 | |
| α-helix | 280-295 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 118-121 | 4 | |
| α-helix | 130-143 | 14 | |
| α-helix | 158-165 | 8 | |
| β-strand | 167 | 1 | 2 |
| β-strand | 169 | 1 | 2 |
| α-helix | 174-176 | 3 | |
| β-strand | 177 | 1 | 1 |
| α-helix | 179-192 | 14 | |
| α-helix | 200-208 | 9 | |
| α-helix | 216-227 | 12 | |
| α-helix | 235-251 | 17 | |
| α-helix | 254-257 | 4 | |
| α-helix | 261-272 | 12 | |
| α-helix | 284-295 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylinositol 3-kinase | A, B | protein | 216 | Homo sapiens | P27986 (AlphaFold model) |
>1PBW_1 PHOSPHATIDYLINOSITOL 3-KINASE (chains A, B) MEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQ LLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLL KKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNT ENLIKVIEILISTEWNERQPAPALPPKPPKPTTVAN
Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. Musacchio, A., Cantley, L.C., Harrison, S.C. Proc Natl Acad Sci U S A (1996) 93:14373-14378. DOI 10.1073/pnas.93.25.14373 · PubMed
Other PDB entries of the same protein (UniProt P27986 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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